Cloning and expression analysis of a novel human serine hydrolase with sequence similarity to prokaryotic enzymes involved in the degradation of aromatic compounds.

摘要: Abstract A full-length cDNA coding for a novel human serine hydrolase has been cloned from breast carcinoma library. Nucleotide sequence analysis shown that the isolated contains an open reading frame polypeptide of 274 amino acids and complete Alu repetitive within its 3′-untranslated region. The predicted acid Gly-X-Ser-X-Gly motif characteristic hydrolases displays extensive similarity to several prokaryotic involved in degradation aromatic compounds. highest degree identities was detected with four encoded by bphD genes different strains Pseudomonas ability degrade biphenyl derivatives. On basis these similarities, this enzyme tentatively called Biphenyl hydrolase-related protein (Bph-rp). Bph-rp expressed Escherichia coli, after purification, recombinant able p-nitrophenylbutyrate, water-soluble substrate commonly used assaying hydrolases. This hydrolytic activity abolished diisopropyl fluorophosphate, covalent inhibitor hydrolases, providing additional evidence encodes member superfamily. Northern blot poly(A) RNAs variety tissues revealed is mainly liver kidney, which also confirmed at level Western antibodies raised against purified Bph-rp. According structural characteristics, tissue distribution Bph-rp, potential role detoxification processes proposed.